Structure of PDB 1wvb Chain A Binding Site BS02
Receptor Information
>1wvb Chain A (length=309) Species:
9606
(Homo sapiens) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
SRTIGIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLP
FADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVKKNGRISLVLGGDHSLA
IGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKG
KIPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVD
RLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTPVVGGLTY
RQGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAITLACF
GLAREGNHK
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
1wvb Chain A Residue 1315 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
1wvb
Subunit-subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acid
Resolution
2.3 Å
Binding residue
(original residue number in PDB)
D124 H126 D232 D234
Binding residue
(residue number reindexed from 1)
D120 H122 D228 D230
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H101 D124 H126 D128 H141 D232 D234 E277
Catalytic site (residue number reindexed from 1)
H97 D120 H122 D124 H137 D228 D230 E273
Enzyme Commision number
3.5.3.1
: arginase.
Gene Ontology
Molecular Function
GO:0004053
arginase activity
GO:0005515
protein binding
GO:0016787
hydrolase activity
GO:0016813
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0030145
manganese ion binding
GO:0046872
metal ion binding
Biological Process
GO:0000050
urea cycle
GO:0002250
adaptive immune response
GO:0006525
arginine metabolic process
GO:0006527
arginine catabolic process
GO:0009624
response to nematode
GO:0019547
arginine catabolic process to ornithine
GO:0042130
negative regulation of T cell proliferation
GO:0042832
defense response to protozoan
GO:0045087
innate immune response
GO:0046007
negative regulation of activated T cell proliferation
GO:0060336
negative regulation of type II interferon-mediated signaling pathway
GO:0070965
positive regulation of neutrophil mediated killing of fungus
GO:2000552
negative regulation of T-helper 2 cell cytokine production
Cellular Component
GO:0005576
extracellular region
GO:0005615
extracellular space
GO:0005634
nucleus
GO:0005737
cytoplasm
GO:0005829
cytosol
GO:0035578
azurophil granule lumen
GO:0035580
specific granule lumen
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:1wvb
,
PDBe:1wvb
,
PDBj:1wvb
PDBsum
1wvb
PubMed
UniProt
P05089
|ARGI1_HUMAN Arginase-1 (Gene Name=ARG1)
[
Back to BioLiP
]